B8ZRB0 (HIS8_MYCLB) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 22.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Histidinol-phosphate aminotransferase EC=2.6.1.9 Alternative name(s): Imidazole acetol-phosphate transaminase | ||||
| Gene names |
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| Organism | Mycobacterium leprae (strain Br4923) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 561304 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 377 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP MF_01023 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP MF_01023 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023 |
| Subunit structure | Homodimer By similarity. HAMAP MF_01023 |
| Sequence similarities | Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Aminotransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activityInferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 377 | 377 | Histidinol-phosphate aminotransferase HAMAP MF_01023 | PRO_1000149107 | |||||
Amino acid modifications | |||||||||
| Modified residue | 230 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Comparative genomic and phylogeographic analysis of Mycobacterium leprae." Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A., Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C., Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H., Vera-Cabrera L. Cole S.T.Nat. Genet. 41:1282-1289(2009) [PubMed: 19881526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Br4923. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FM211192 Genomic DNA. Translation: CAR71353.1. |
| RefSeq | YP_002503537.1. NC_011896.1. |
3D structure databases | |
| ProteinModelPortal | B8ZRB0. |
| SMR | B8ZRB0. Positions 7-368. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B8ZRB0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000087006; EBMYCP00000083014; EBMYCG00000085270. |
| GeneID | 7324682. |
| GenomeReviews | Gene locus MLBr01258 in contig FM211192_GR. |
| PATRIC | 18044212. VBIMycLep121698_2330. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00070000031717. |
| HOGENOM | HBG646350. |
| OMA | ATATEWV. |
| ProtClustDB | PRK03317. |
Family and domain databases | |
| HAMAP | MF_01023. HisC_aminotrans_2. [Tree] |
| InterPro | IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit. |
| Pfam | PF00155. Aminotran_1_2. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| TIGRFAMs | TIGR01141. HisC. 1 hit. |
| PROSITE | PS00599. AA_TRANSFER_CLASS_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HIS8_MYCLB | ||||||||
| Accession | Primary (citable) accession number: B8ZRB0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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